Amino acid sequencing of a trypsin inhibitor by refined 1.6 Å X-ray crystal structure of its complex with porcine β-trypsin
| Autor: | Youqi Tang, Shengping Liu, Qichen Huang, Rui-Qing Qian, Fu-Yue Zeng |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Protein Conformation
Swine Stereochemistry Trypsin inhibitor Molecular Sequence Data Biophysics Crystal structure Biochemistry Scissile bond X-Ray Diffraction Structural Biology Complex Genetics medicine Animals Trypsin Molecular replacement Amino Acid Sequence Molecular Biology Plant Proteins chemistry.chemical_classification biology Cell Biology Amino acid Crystallography sequencing Bond length Crystallography chemistry Enzyme inhibitor Active site geometry biology.protein Trypsin Inhibitors Momordica charantia Linn trypsin inhibitor-A medicine.drug |
| Zdroj: | FEBS Letters. 297:143-146 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(92)80346-i |
| Popis: | The stoichiometric complex formed between porcine β-trypsin and the Momordica charantia , Linn. Cucurbitaceae trypsin inhibitor-A (MCTI-A) was crystallized and its X-ray crystal structure determined using molecular replacement method. The primary sequence and topology of the inhibitor was determined by recognizing the electron density and refined to a final R value of 0.167 (7.0—1.6 A) with RMS deviation of bond lengths from standard values 0.012 A. The sequence was compared with those obtained by other groups and was found to be similar to the squash proteinase inhibitor. Its spatial structure and the conformation of its primary binding segment from Cys-31 (P3) to Glu-71 (P3′) which contains the reactive scissile bond Arg-51 C-Ile-61 N were also very similar with other squash family proteinase inhibitors. |
| Databáze: | OpenAIRE |
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